Collagen is a ubiquitous material living organisms use to create structure through the self-assembly of fibrillogenic proteins. It is desirable to design improved materials with biological, chemical, and mechanical properties that mimic collage as it is typically biocompatible. The triple-helical domain of native collagen comprises a recurrence of a tripeptide repeat sequence Xaa-Yaa-Gly. The amino acids in the Xaa and Yaa positions vary; however from a statistical standpoint, Proline (Pro) and (4R)-hydroxyproline (Hyp), respectively, most frequently occupy the these positions. The assembly of synthetic collagen triple helices has been reported. See, e.g., Rele et al. JACS, 2007, 129, 14780-14787; Gauba et al., JACS, 2008, 130(23):7509-7515; Russell et al., JACS, 2010, 132 (10):3242-3243; O'Leary et al., Nature Chemistry, 2011, 3, 821-828, O'Leary et al., JACS, 2011, 133 (14), 5432-5443; and Fallas et al., JACS, 2012, 134 (3):1430-1433.
The self-assembly of synthetic collagen into two or three dimensional structures desirable for fabricating artificial medical devices or implantable material has been challenging. Thus, there is a need to identify improved materials. Przybyla et al. report hierarchical assembly of collagen peptide triple helices into curved disks and metal ion-promoted hollow spheres. JACS, 2013, 135 (9):3418-3422. Xu et al., report self-Assembly of left- and right-handed molecular screws. JACS, 2013, 135 (50):18762-18765.
Babu & Ganesh report collagen peptides with 4R-aminoprolyl (Amp) residues. JACS, 2001, 123(9):2079-80. See also Umashankara et al., Chem Commun (Camb), 2003, (20):2606-7.
Arginine-coated peptides are reported to self-assemble to nanosheets in water. Hamley et al., Chem Commun (Camb), 2013, 49(18):1850-2.
References cited herein are not an admission of prior art.